A0A2R6R5E7 · A0A2R6R5E7_ACTCC

Function

function

Removal of H2O2, oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Binds 2 calcium ions per subunit.
heme b (UniProtKB | Rhea| CHEBI:60344 )

Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.

Features

Showing features for site, active site, binding site.

TypeIDPosition(s)Description
Site64Transition state stabilizer
Active site68Proton acceptor
Binding site69Ca2+ 1 (UniProtKB | ChEBI)
Binding site72Ca2+ 1 (UniProtKB | ChEBI)
Binding site74Ca2+ 1 (UniProtKB | ChEBI)
Binding site76Ca2+ 1 (UniProtKB | ChEBI)
Binding site78Ca2+ 1 (UniProtKB | ChEBI)
Binding site90Ca2+ 1 (UniProtKB | ChEBI)
Binding site168substrate
Binding site198Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue
Binding site199Ca2+ 2 (UniProtKB | ChEBI)
Binding site250Ca2+ 2 (UniProtKB | ChEBI)
Binding site253Ca2+ 2 (UniProtKB | ChEBI)
Binding site258Ca2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functionheme binding
Molecular Functionlactoperoxidase activity
Molecular Functionmetal ion binding
Biological Processhydrogen peroxide catabolic process
Biological Processresponse to oxidative stress

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Peroxidase
  • EC number

Gene names

    • ORF names
      CEY00_Acc10282

Organism names

Accessions

  • Primary accession
    A0A2R6R5E7

Proteomes

Genome annotation databases

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

TypeIDPosition(s)Description
Signal1-26
ChainPRO_501521676527-330Peroxidase
Disulfide bond37↔120
Disulfide bond70↔75
Disulfide bond126↔326
Disulfide bond205↔237

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain27-330Plant heme peroxidase family profile

Sequence similarities

Belongs to the peroxidase family. Ascorbate peroxidase subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    330
  • Mass (Da)
    35,661
  • Last updated
    2018-06-20 v1
  • Checksum
    FF4E07D08E8107E3
MSRFNILVALWSVSLCLSIFPNLASAQLKQNYYAKICPNVETIVRNAVTQKFKQTFVTVPATLRLFFHDCFVQGCDASVIIASSGNNQAEKDHPDNLSLAGDGFDTVIKAKAAVDAVASCRNKVSCADILAMATRDVIALSGGPSYEVELGRLDGLSSTAASVNGNLPQPTFNLKQLHSMFVSHGLTQADMIALSAAHTVGFSHCSKFANRIYNFSRENPVDPTLDKAYAAQLQSMCPKNVDPRIAINMDPNTPNTFDNVYFQNLQQGKGLFTSDQVLFTDSRSKPTVDAWAGNSPAFQKAFITAITKLGRVGVKTGANGNIRTDCSAFN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NKQK01000009
EMBL· GenBank· DDBJ
PSS21238.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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